ID CTNS_MOUSE Reviewed; 367 AA. AC P57757; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 1. DT 24-JAN-2024, entry version 149. DE RecName: Full=Cystinosin {ECO:0000303|PubMed:11121245}; DE Flags: Precursor; GN Name=Ctns {ECO:0000303|PubMed:11121245, ECO:0000312|MGI:MGI:1932872}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11121245; DOI=10.1186/1471-2164-1-2; RA Cherqui S., Kalatzis V., Forestier L., Poras I., Antignac C.; RT "Identification and characterisation of the murine homologue of the gene RT responsible for cystinosis, Ctns."; RL BMC Genomics 1:2-2(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=12370309; DOI=10.1128/mcb.22.21.7622-7632.2002; RA Cherqui S., Sevin C., Hamard G., Kalatzis V., Sich M., Pequignot M.O., RA Gogat K., Abitbol M., Broyer M., Gubler M.C., Antignac C.; RT "Intralysosomal cystine accumulation in mice lacking cystinosin, the RT protein defective in cystinosis."; RL Mol. Cell. Biol. 22:7622-7632(2002). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=17977621; DOI=10.1016/j.neurobiolaging.2007.09.006; RA Maurice T., Hippert C., Serratrice N., Dubois G., Jacquet C., Antignac C., RA Kremer E.J., Kalatzis V.; RT "Cystine accumulation in the CNS results in severe age-related memory RT deficits."; RL Neurobiol. Aging 30:987-1000(2009). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=21897743; RA Simpson J., Nien C.J., Flynn K., Jester B., Cherqui S., Jester J.; RT "Quantitative in vivo and ex vivo confocal microscopy analysis of corneal RT cystine crystals in the Ctns knockout mouse."; RL Mol. Vis. 17:2212-2220(2011). RN [8] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22649030; DOI=10.1096/fj.11-201376; RA Chiaverini C., Sillard L., Flori E., Ito S., Briganti S., Wakamatsu K., RA Fontas E., Berard E., Cailliez M., Cochat P., Foulard M., Guest G., RA Niaudet P., Picardo M., Bernard F.X., Antignac C., Ortonne J.P., RA Ballotti R.; RT "Cystinosin is a melanosomal protein that regulates melanin synthesis."; RL FASEB J. 26:3779-3789(2012). RN [9] RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH V-ATPASE AND RAGULATOR RP COMPLEXES, INTERACTION WITH RRAGA AND RRAGC, AND MUTAGENESIS OF LYS-280. RX PubMed=26449607; DOI=10.1681/asn.2014090937; RA Andrzejewska Z., Nevo N., Thomas L., Chhuon C., Bailleux A., Chauvet V., RA Courtoy P.J., Chol M., Guerrera I.C., Antignac C.; RT "Cystinosin is a component of the vacuolar H+-ATPase-Ragulator-Rag complex RT controlling mammalian target of rapamycin complex 1 signaling."; RL J. Am. Soc. Nephrol. 27:1678-1688(2016). RN [10] RP FUNCTION, AND MUTAGENESIS OF LYS-280. RX PubMed=28465352; DOI=10.1074/jbc.m116.764076; RA Zhang J., Johnson J.L., He J., Napolitano G., Ramadass M., Rocca C., RA Kiosses W.B., Bucci C., Xin Q., Gavathiotis E., Cuervo A.M., Cherqui S., RA Catz S.D.; RT "Cystinosin, the small GTPase Rab11, and the Rab7 effector RILP regulate RT intracellular trafficking of the chaperone-mediated autophagy receptor RT LAMP2A."; RL J. Biol. Chem. 292:10328-10346(2017). CC -!- FUNCTION: Cystine/H(+) symporter that mediates export of cystine, the CC oxidized dimer of cysteine, from lysosomes (PubMed:12370309). Plays an CC important role in melanin synthesis by catalyzing cystine export from CC melanosomes, possibly by inhibiting pheomelanin synthesis CC (PubMed:22649030). In addition to cystine export, also acts as a CC positive regulator of mTORC1 signaling in kidney proximal tubular CC cells, via interactions with components of the v-ATPase and Ragulator CC complexes (PubMed:26449607). Also involved in small GTPase-regulated CC vesicle trafficking and lysosomal localization of LAMP2A, independently CC of cystine transporter activity (PubMed:28465352). CC {ECO:0000269|PubMed:12370309, ECO:0000269|PubMed:22649030, CC ECO:0000269|PubMed:26449607, ECO:0000269|PubMed:28465352}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in); CC Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491; CC Evidence={ECO:0000250|UniProtKB:O60931}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173; CC Evidence={ECO:0000250|UniProtKB:O60931}; CC -!- ACTIVITY REGULATION: Switches between a lumen- and a cytosol-open CC conformation: pH induces conformational changes and shifts the CC equilibrium to facilitate the transition between the lumen- and CC cytosol-open conformation, thereby promoting cystine transport. CC Protonation of specific aspartate residues (Asp-205, Asp-305 and Asp- CC 346) favors the cytosol-open conformation. CC {ECO:0000250|UniProtKB:O60931}. CC -!- SUBUNIT: Interacts with components of the V-ATPase complex CC (PubMed:26449607). Interacts with components of the Ragulator complex CC (PubMed:26449607). Interacts with RRAGA/RagA and RRAGC/RagC CC (PubMed:26449607). Interacts with AP-3 complex subunit mu (AP3M1 or CC AP3M2) (By similarity). {ECO:0000250|UniProtKB:O60931, CC ECO:0000269|PubMed:26449607}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:12370309}; CC Multi-pass membrane protein {ECO:0000255}. Melanosome membrane CC {ECO:0000250|UniProtKB:O60931}; Multi-pass membrane protein CC {ECO:0000255}. Note=AP-3 complex is required for localization to the CC lysosome. {ECO:0000250|UniProtKB:O60931}. CC -!- DOMAIN: The lysosomal targeting motif, together with te second PQ-loop CC mediate targeting to the lysosome. {ECO:0000250|UniProtKB:O60931}. CC -!- DISRUPTION PHENOTYPE: Mice develop ocular damages, bone defects and CC behavioral anomalies (PubMed:12370309). Defects are caused by cystine CC accumulation in all organs tested, and formation of cystine crystals CC (PubMed:12370309). Mice do not develop signs of a proximal tubulopathy CC or renal failure (PubMed:12370309). Cystine accumulation in the central CC nervous system causes severe age-related memory deficits: spatial CC reference and working memory deficits are observed in middle-aged mice CC (PubMed:17977621). In eyes, cystine crystals induce inflammatory and CC immune response with aging associated with loss of keratocyte and CC endothelial cells (PubMed:21897743). Mice show a strong increase in CC hair pheomelanin content (PubMed:22649030). Decreased mTORC1 signaling CC pathway in proximal tubular cell lines (PubMed:26449607). CC {ECO:0000269|PubMed:12370309, ECO:0000269|PubMed:17977621, CC ECO:0000269|PubMed:21897743, ECO:0000269|PubMed:22649030, CC ECO:0000269|PubMed:26449607}. CC -!- SIMILARITY: Belongs to the cystinosin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ250670; CAC19455.1; -; mRNA. DR EMBL; AK078511; BAC37316.1; -; mRNA. DR EMBL; BC005479; AAH05479.1; -; mRNA. DR CCDS; CCDS25001.1; -. DR RefSeq; NP_112541.1; NM_031251.4. DR RefSeq; XP_006534596.1; XM_006534533.3. DR RefSeq; XP_006534597.1; XM_006534534.3. DR AlphaFoldDB; P57757; -. DR SMR; P57757; -. DR STRING; 10090.ENSMUSP00000104116; -. DR GlyCosmos; P57757; 6 sites, No reported glycans. DR GlyGen; P57757; 6 sites. DR iPTMnet; P57757; -. DR PhosphoSitePlus; P57757; -. DR PaxDb; 10090-ENSMUSP00000006103; -. DR ProteomicsDB; 284146; -. DR Antibodypedia; 23081; 210 antibodies from 27 providers. DR DNASU; 83429; -. DR Ensembl; ENSMUST00000006103.9; ENSMUSP00000006103.3; ENSMUSG00000005949.10. DR Ensembl; ENSMUST00000108476.8; ENSMUSP00000104116.2; ENSMUSG00000005949.10. DR GeneID; 83429; -. DR KEGG; mmu:83429; -. DR UCSC; uc007kae.1; mouse. DR AGR; MGI:1932872; -. DR CTD; 1497; -. DR MGI; MGI:1932872; Ctns. DR VEuPathDB; HostDB:ENSMUSG00000005949; -. DR eggNOG; KOG3145; Eukaryota. DR GeneTree; ENSGT00390000005338; -. DR HOGENOM; CLU_046327_1_0_1; -. DR InParanoid; P57757; -. DR OMA; WIDVIYT; -. DR OrthoDB; 179669at2759; -. DR PhylomeDB; P57757; -. DR TreeFam; TF313589; -. DR Reactome; R-MMU-425393; Transport of inorganic cations/anions and amino acids/oligopeptides. DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events. DR BioGRID-ORCS; 83429; 3 hits in 78 CRISPR screens. DR ChiTaRS; Ctns; mouse. DR PRO; PR:P57757; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P57757; Protein. DR Bgee; ENSMUSG00000005949; Expressed in lip and 173 other cell types or tissues. DR ExpressionAtlas; P57757; baseline and differential. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005770; C:late endosome; ISO:MGI. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0042470; C:melanosome; ISS:UniProtKB. DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IDA:MGI. DR GO; GO:0015295; F:solute:proton symporter activity; ISS:UniProtKB. DR GO; GO:0007628; P:adult walking behavior; IMP:MGI. DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI. DR GO; GO:0007420; P:brain development; ISO:MGI. DR GO; GO:1904970; P:brush border assembly; ISO:MGI. DR GO; GO:0050890; P:cognition; ISO:MGI. DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI. DR GO; GO:0007625; P:grooming behavior; IMP:MGI. DR GO; GO:0015811; P:L-cystine transport; IDA:MGI. DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI. DR GO; GO:0007616; P:long-term memory; IMP:MGI. DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; ISO:MGI. DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI. DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI. DR GO; GO:2000611; P:positive regulation of thyroid hormone generation; ISO:MGI. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0072158; P:proximal tubule morphogenesis; ISO:MGI. DR GO; GO:0048021; P:regulation of melanin biosynthetic process; ISS:UniProtKB. DR GO; GO:0097018; P:renal albumin absorption; ISO:MGI. DR GO; GO:0035623; P:renal glucose absorption; ISO:MGI. DR GO; GO:0097291; P:renal phosphate ion absorption; ISO:MGI. DR GO; GO:0070295; P:renal water absorption; ISO:MGI. DR GO; GO:0030878; P:thyroid gland development; ISO:MGI. DR GO; GO:0008542; P:visual learning; IMP:MGI. DR Gene3D; 1.20.1280.290; -; 1. DR InterPro; IPR005282; LC_transporter. DR InterPro; IPR006603; PQ-loop_rpt. DR NCBIfam; TIGR00951; 2A43; 1. DR PANTHER; PTHR13131; CYSTINOSIN; 1. DR PANTHER; PTHR13131:SF5; CYSTINOSIN; 1. DR Pfam; PF04193; PQ-loop; 2. DR SMART; SM00679; CTNS; 2. DR Genevisible; P57757; MM. PE 1: Evidence at protein level; KW Glycoprotein; Lysosome; Melanin biosynthesis; Membrane; Protein transport; KW Reference proteome; Repeat; Signal; Symport; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1..22 FT /evidence="ECO:0000250|UniProtKB:O60931" FT CHAIN 23..367 FT /note="Cystinosin" FT /id="PRO_0000205515" FT TOPO_DOM 23..125 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TRANSMEM 126..150 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TOPO_DOM 151..159 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TRANSMEM 160..179 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TOPO_DOM 180..202 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O60931, ECO:0000305" FT TRANSMEM 203..225 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TOPO_DOM 226..234 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TRANSMEM 235..257 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TOPO_DOM 258..263 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O60931, ECO:0000305" FT TRANSMEM 264..289 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TOPO_DOM 290..298 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TRANSMEM 299..308 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TOPO_DOM 309..331 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TRANSMEM 332..354 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:O60931" FT TOPO_DOM 355..367 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O60931" FT DOMAIN 123..189 FT /note="PQ-loop 1" FT DOMAIN 263..328 FT /note="PQ-loop 2" FT MOTIF 362..366 FT /note="Lysosomal targeting motif" FT /evidence="ECO:0000255" FT BINDING 166 FT /ligand="L-cystine" FT /ligand_id="ChEBI:CHEBI:35491" FT /evidence="ECO:0000250|UniProtKB:O60931" FT BINDING 205 FT /ligand="H(+)" FT /ligand_id="ChEBI:CHEBI:15378" FT /evidence="ECO:0000250|UniProtKB:O60931" FT BINDING 273 FT /ligand="L-cystine" FT /ligand_id="ChEBI:CHEBI:35491" FT /evidence="ECO:0000250|UniProtKB:O60931" FT BINDING 280 FT /ligand="L-cystine" FT /ligand_id="ChEBI:CHEBI:35491" FT /evidence="ECO:0000250|UniProtKB:O60931" FT BINDING 281 FT /ligand="L-cystine" FT /ligand_id="ChEBI:CHEBI:35491" FT /evidence="ECO:0000250|UniProtKB:O60931" FT BINDING 305 FT /ligand="H(+)" FT /ligand_id="ChEBI:CHEBI:15378" FT /note="protonated residue following cystine-binding" FT /evidence="ECO:0000250|UniProtKB:O60931" FT BINDING 305 FT /ligand="L-cystine" FT /ligand_id="ChEBI:CHEBI:35491" FT /evidence="ECO:0000250|UniProtKB:O60931" FT BINDING 346 FT /ligand="H(+)" FT /ligand_id="ChEBI:CHEBI:15378" FT /evidence="ECO:0000250|UniProtKB:O60931" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 66 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 84 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT MUTAGEN 280 FT /note="K->R: Abolished cystine transport. Abolished FT interaction with components of the v-ATPase and Ragulator FT complexes. Does not affect ability to lysosomal FT localization of LAMP2A." FT /evidence="ECO:0000269|PubMed:26449607, FT ECO:0000269|PubMed:28465352" SQ SEQUENCE 367 AA; 42203 MW; 651DF351189C419E CRC64; MRRNWLLILT LFLLMFIEKY ESTVSLTAPP TVKLENGSST NVDITLGHPL NSTLVITFEV TFRSKNLTIV ELPDEVIVPR GEKNASFQVT SQNIGQVTVF LHGNHSNQTC PRIRFLVIHS RIVSIINQVI GWIYFMAWSV SFYPQVIQNW RRKSVIGLSF DFLALNLTGF VAYSVFNIGL LWVPYIQEEF LLKYPNGVNP VDSNDAFFSL HAVALTLIVI LQCCLYERGN QRVSWPSIGF LVLAWLFVLV TMIVAAVGIT TWLQFLFCFS YIKLIITLIK YFPQAYMNFY YKSTKGWSIG GVLLDFTGGS FSLLQMFLQS YNNDQWTLIF GDPTKFGLGV FTIFFDVVFF IQHFYLYRKK PGYDQLN //